Dr John Rafferty
School of Biosciences
Reader in Structural Biology
Principal Admissions Tutor
+44 114 222 2809
Full contact details
School of Biosciences
Firth Court
Western Bank
91直播
S10 2TN
- Profile
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Career history
- 2005 - present: Reader in Structural Biology, School of Biosciences, 91直播 Univ
- 1999 - 2004: Royal Society Olga Kennard Fellow, Mol.Biol.&Biotech.Dept, 91直播 Univ
- 1996 - 1999: BBSRC David Phillips Research Fellow, Mol.Biol.&Biotech.Dept, 91直播 Univ.
- 1992 - 1996: PDRA, Mol.Biol. & Biotech. Dept, 91直播 Univ.
- 1990 - 1991: PDRA, Biochem. & Mol.Biol. Dept, Leeds Univ.
- 1989 - 1990: PDRA, Biophysics Dept, Leeds Univ.
- 1986 - 1990: PhD, Biophysics Dept, Leeds Univ.
- Research interests
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My research interests centre on structural studies of proteins and nucleic acids primarily by X-ray crystallography but also utilizing other biophysical techniques such as NMR, SAXS and electron microscopy.
The work provides detailed 3-dimensional insights into biological macromolecules and their assemblies that can be combined with biochemical and genetic investigations to provide a better understanding of how they function.
Currently my research includes determining structural details of proteins involved in DNA or RNA binding; proteins from bacterial membrane transport systems; toxin & antitoxin proteins; and glycosidic enzymes.
The structure of MatC, with its helices and strands shown as cartoon coils and arrows, and a bound D-malate substrate, shown in stick form.
The protein has a hinged 鈥淰enus-flytrap-like鈥 structure, with a cleft where the substrate is coordinated, separating two globular domains (the helices and strands for the first domain are shown in cyan and magenta and for the second domain in red and orange). (Rosa et al. (2019) J. Mol. Biol. 431, 351-367)
DNA & RNA metabolism
Drawing originally from work on E.coli DNA recombination protein RuvA and its DNA junction complex, my group has focussed on the recognition and processing of junction points in DNA.
The work has involved studies of proteins from a diverse range of bacterial and viral sources.
It has also expanded into structural studies of RNA binding proteins from bacterial pathogens and simple eukaryotes that regulate the assembly of the ribosome.
In parallel with the crystallography, we have examined the solution structures by SAXS.
Host-pathogen interactions
Recently we have carried out successful and exciting studies of proteins from the pathogen Campylobacter jejuni, which is the major cause of food poisoning worldwide.
This work has seen structures determined for proteins from the bacterial periplasm responsible for metabolite transport across the inner membrane, protein folding & establishment of the outer membrane and mechanisms for avoiding the host immune system.
The work has been extended to examine proteins from the periplasm of other organisms such as Rhodopseudomonas palustris, which is of interest because of its potential biotechnological role in lignin processing.
Glycoside recognition and processing
The carbohydrate coat on many cells provides both a protective role but also a nutrient source for invading organisms.
We have been studying the structural determinants that control the way key enzymes and associated binding domains recognize specific targets and process them.
These proteins in pathogenic organisms provide potentially excellent targets for inhibition and the development of antibacterial compounds.
- Publications
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- Teaching activities
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Level 3 modules
- MBB344 Genomic Science
- MBB362 Biochemistry Data Handling
Level 2 modules
- MBB261 Biochemistry 2
- MBB265 Practical Molecular Bioscience 2
Level 1 modules
- MBB161 Biochemistry (Module Coordinator)
- MBB165 Practical Molecular Bioscience 1